Advanced Search

Journal Navigation

Journal Home

Subscriptions

Archive

Contact Us

Table of Contents

Click here for more information

Click here to sign up for SAGE Journal Email Alerts today!

Sign In to gain access to subscriptions and/or personal tools.
Journal of Dental Research
This Article
Right arrow Free Full Text (Free PDF) Free
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to Saved Citations
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Request Reprints
Right arrow Add to My Marked Citations
Citing Articles
Right arrow Citing Articles via Google Scholar
Right arrow Citing Articles via Scopus
Google Scholar
Right arrow Articles by Vadeboncoeur, C.
Right arrow Articles by Trahan, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vadeboncoeur, C.
Right arrow Articles by Trahan, L.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*GLUCOSE
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

A Comparative Study of Enzymes Involved in Glucose Phosphorylation in Oral Streptococci

C. Vadeboncoeur

School of Dental Medicine and Department of Biochemistry, Faculty of Sciences, Laval University, Quebec, Canada GIK 7P4

D. Mayrand

School of Dental Medicine and Department of Biochemistry, Faculty of Sciences, Laval University, Quebec, Canada GIK 7P4

L. Trahan

School of Dental Medicine and Department of Biochemistry, Faculty of Sciences, Laval University, Quebec, Canada GIK 7P4

The properties of two enzymes involved in the phosphorylation of glucose were studied in three oral streptococci species. The glucokinase of Streptococcus mutans had a lower affinity for glucose and ATP than did those from S. salivarius and S. sanguis. The enzyme had an identical pH optimum (pH 8.0) in all three bacteria. However, the results from the phosphoenolpyruvate phosphotransferase system showed a different pattern when its activity was measured using 2-deoxyglucose with toluenized cells. Uptake studies of 2-deoxyglucose also revealed that the three microorganisms had different affinities for this compound. This glucose analogue strongly inhibited the acid production of S. salivarius, but did not affect the glycolysis of the other two bacteria.

Journal of Dental Research, Vol. 61, No. 1, 60-65 (1982)
DOI: 10.1177/00220345820610011401
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?